› 5uro

X-ray diffraction
1.7Å resolution

Structure of a soluble epoxide hydrolase identified in Trichoderma reesei

Released:
DOI: 10.2210/pdb5uro/pdb
PDB entry 5uro coloured by chain, front view.
PDB entry 5uro coloured by chain, side view.
PDB entry 5uro coloured by chain, top view.
Source organism: Trichoderma reesei QM6a
Primary publication:
Structure of a soluble epoxide hydrolase identified in Trichoderma reesei.
Wilson C, De Oliveira GS, Adriani PP, Chambergo FS, Dias MVB
Biochim Biophys Acta Proteins Proteom 1865 1039-1045 (2017)
PMID: 28502798

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123861 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 336 amino acids
Theoretical weight: 37.53 KDa
Source organism: Trichoderma reesei QM6a
Expression system: Escherichia coli 55989
UniProt:
  • Canonical: G0R7E2 (Residues: 1-335; Coverage: 98%)
Gene name: TRIREDRAFT_53220
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments

1 bound ligand:
Ligand 8LD 1 x 8LD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Unit cell:
a: 51.427Å b: 78.281Å c: 87.372Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.211
Expression system: Escherichia coli 55989

Quick links

Citations

3 citation in other articles

Identification and catalytic properties of new epoxide hydrolases from the genomic data of soil bacteria.
Stojanovski et al. (2020)
2 more

4 mentions without citation

Evolution of tunnels in α/β-hydrolase fold proteins-What can we learn from studying epoxide hydrolases?
Bzówka et al. (2022)
3 more